The Phytophthora sojae RXLR effector Avh238 destabilizes soybean Type2 GmACSs to suppress ethylene biosynthesis and promote infection

New Phytol. 2019 Apr;222(1):425-437. doi: 10.1111/nph.15581. Epub 2018 Nov 27.

Abstract

Phytophthora pathogens secrete many effector proteins to manipulate host innate immunity. PsAvh238 is a Phytophthora sojae N-terminal Arg-X-Leu-Arg (RXLR) effector, which evolved to escape host recognition by mutating one nucleotide while retaining plant immunity-suppressing activity to enhance infection. However, the molecular basis of the PsAvh238 virulence function remains largely enigmatic. By using coimmunoprecipitation and liquid chromatography-tandem mass spectrometry analysis, we identified the 1-aminocyclopropane-1-carboxylate synthase (ACS) isoforms, the key enzymes in ethylene (ET) biosynthesis, as a host target of PsAvh238. We show that PsAvh238 interacts with soybean ACSs (GmACSs) in vivo and in vitro. By destabilizing Type2 GmACSs, PsAvh238 suppresses Type2 ACS-catalyzed ET biosynthesis and facilitates Phytophthora infection. Silencing of Type2 GmACSs, and inhibition of ET biosynthesis or signaling, increase soybean susceptibility to P. sojae infection, supporting a role for Type2 GmACSs and ET in plant immunity against P. sojae. Moreover, wild-type P. sojae but not the PsAvh238-disrupted mutants, inhibits ET induction and promotes P. sojae infection in soybean. Our results highlight the ET biosynthesis pathway as an essential part in plant immunity against P. sojae and a direct effector target.

Keywords: Phytophthora sojae; RXLR effector; Type2 ACS; ethylene; plant immunity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Disease Resistance
  • Enzyme Stability
  • Ethylenes / metabolism*
  • Gene Silencing
  • Glycine max / immunology
  • Glycine max / metabolism*
  • Glycine max / microbiology*
  • Lyases / metabolism*
  • Mutation / genetics
  • Nicotiana / genetics
  • Nicotiana / microbiology
  • Phytophthora / physiology*
  • Plant Diseases / microbiology*
  • Plants, Genetically Modified
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Binding
  • Proteins / metabolism*

Substances

  • Ethylenes
  • Proteins
  • Proteasome Endopeptidase Complex
  • Lyases
  • 1-aminocyclopropanecarboxylate synthase

Associated data

  • GENBANK/698504359